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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Biocatalyst engineering of Thermomyces Lanuginosus lipase adsorbed on hydrophobic supports: Modulation of enzyme properties for ethanolysis of oil in solvent-free systems

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Author(s):
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Silveira, Erick Abreu [1, 2] ; Moreno-Perez, Sonia [3] ; Basso, Alessandra [4] ; Serban, Simona [4] ; Pestana-Mamede, Rita [2] ; Tardioli, Paulo W. [1] ; Sanchez-Farinas, Cristiane [5] ; Castejon, Natalia [6] ; Fernandez-Lorente, Gloria [2] ; Rocha-Martin, Javier [2] ; Guisan, Jose M. [2]
Total Authors: 11
Affiliation:
[1] Univ Fed Sao Carlos, Sao Carlos, SP - Brazil
[2] CSIC, ICP, Dept Biocatalysis, Campus UAM, Madrid 28049 - Spain
[3] Univ Europea Madrid, Sch Biomed Sci, Pharm & Biotechnol Dept, Madrid - Spain
[4] Purolite, Unit D, Llantrisant Business Pk, Llantrisant CF72 8LF, South Wales - Wales
[5] Embrapa Instrumentat, Sao Carlos, SP - Brazil
[6] Univ Autonoma Madrid, Fac Sci, Secc Dept Ciencias Alimentac, Hlth Lipids Grp, E-28049 Madrid - Spain
Total Affiliations: 6
Document type: Journal article
Source: Journal of Biotechnology; v. 289, p. 126-134, JAN 10 2019.
Web of Science Citations: 2
Abstract

Different immobilized biocatalysts of Thermomyces lanuginosus lipase (TLL) exhibited different properties for the ethanolysis of high oleic sunflower oil in solvent-free systems. TLL immobilized by interfacial adsorption on octadecyl (C-18) supports lost its 1,3-regioselectivity and produced more than 99% of ethyl esters. This reaction was influenced by mass-transfer limitations. TLL adsorbed on macroporous C-18 supports (616 A of pore diameter) was 10-fold more active than TLL adsorbed on mesoporous supports (100-200 A of pore diameter) in solvent-free systems. Both derivatives exhibited similar activity when working in hexane in the absence of diffusional limitations. In addition, TLL adsorbed on macroporous Purolite C-18 was 5-fold more stable than TLL adsorbed on mesoporous Sepabeads C-18. The stability of the best biocatalyst was 20-fold lower in anhydrous oil than in anhydrous hexane. Mild PEGylation of immobilized TLL greatly increased its stability in anhydrous hexane at 40 degrees C, fully preserving the activity after 20 days. In anhydrous oil at 40 degrees C, PEGylated TLL-Purolite C18 retained 65% of its initial activity after six days compared to 10% of the activity retained by the unmodified biocatalyst. Macroporous and highly hydrophobic supports (e. g., Purolite C-18) seem to be very useful to prepare optimal immobilized biocatalysts for ethanolysis of oils by TLL in solvent-free systems. (AU)

FAPESP's process: 13/20826-0 - Production of lipase by the combined fermentation process and its application in the modification of oils and fats
Grantee:Erick de Abreu Silveira
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 15/10530-2 - Application of different enzyme engineering strategies to obtain derivatives of new immobilized-stabilized lipases
Grantee:Erick de Abreu Silveira
Support type: Scholarships abroad - Research Internship - Doctorate
FAPESP's process: 16/10636-8 - From the cell factory to the Biodiesel-Bioethanol integrated biorefinery: a systems approach applied to complex problems in micro and macroscales
Grantee:Roberto de Campos Giordano
Support type: Program for Research on Bioenergy (BIOEN) - Thematic Grants